ID A0A0W0WW75_9GAMM Unreviewed; 550 AA.
AC A0A0W0WW75;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Probable protein kinase UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
DE EC=2.7.-.- {ECO:0000256|HAMAP-Rule:MF_00414};
DE AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000256|HAMAP-Rule:MF_00414};
GN Name=ubiB {ECO:0000256|HAMAP-Rule:MF_00414,
GN ECO:0000313|EMBL:KTD36574.1};
GN ORFNames=Lnau_1558 {ECO:0000313|EMBL:KTD36574.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36574.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD36574.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36574.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity which
CC is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis [regulation].
CC {ECO:0000256|ARBA:ARBA00005020, ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00414};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000256|ARBA:ARBA00009670}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00414}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD36574.1}.
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DR EMBL; LNYO01000013; KTD36574.1; -; Genomic_DNA.
DR RefSeq; WP_058504557.1; NZ_LNYO01000013.1.
DR AlphaFoldDB; A0A0W0WW75; -.
DR STRING; 45070.Lnau_1558; -.
DR PATRIC; fig|45070.6.peg.1633; -.
DR OrthoDB; 9795390at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13972; UbiB; 1.
DR HAMAP; MF_00414; UbiB; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR010232; UbiB.
DR InterPro; IPR045308; UbiB_bact.
DR NCBIfam; TIGR01982; UbiB; 1.
DR PANTHER; PTHR10566; CHAPERONE-ACTIVITY OF BC1 COMPLEX CABC1 -RELATED; 1.
DR PANTHER; PTHR10566:SF129; PROTEIN KINASE UBIB-RELATED; 1.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Kinase {ECO:0000256|HAMAP-Rule:MF_00414};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00414};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00414};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00414}; Ubiquinone {ECO:0000313|EMBL:KTD36574.1};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_00414}.
FT TRANSMEM 498..521
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT TRANSMEM 527..544
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT DOMAIN 93..342
FT /note="ABC1 atypical kinase-like"
FT /evidence="ECO:0000259|Pfam:PF03109"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 130..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00414"
SQ SEQUENCE 550 AA; 63839 MW; D2A91DF3882E75DA CRC64;
MKSIKQLLRL LHINTILARN GLDQVVVSIR LFSPFRFIVY LNPWNWLRKE KLTRGEALRK
TLEELGPIFI KFGQALSTRP DILPPDIAQE LCKLQDKVPP FPSDIALKIV ESAFGRSAYD
VFAQFDPHPL ASASMAQVHT AILHSGEEVV VKILRPNMRK IIEKDLSIMY TIANLADRYW
AESKRLKPKE IVREFEHNLF DELDLQREAA NAGQLRRNFH NSPLLYIPEI YWDYTRENVM
VMERIHGIPV SDLATLQANN INIKKLAERG VEIFFTQVFR DCFFHADMHP GNIFVSPEFP
DNPQYICIDF GIIGTLNDSD KRYLAENLYA FFNRDYRRVA QLHVESGWVA RDTRVEEFES
AIRTVCEPIF EKPLKDISFA QVVLRLFQVA RRFQMEVQPQ LVLLQKTLLA IEGLGRQLYP
ELDLWATAKP FLEKWLKEQI GPKAFFRQLR ENLPFLTEQL PHMPRLIHEV LELTKEQKIR
ALEQHKIRDH SFRSQKNWYK GLGVGIFTTM ITVSLLSYLN VLNYDKLAPT ALLVAVAGGF
ISLINRTTRS
//
